QUEF_STRTD
ID QUEF_STRTD Reviewed; 163 AA.
AC Q03L13;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00818};
DE AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818};
GN Name=queF {ECO:0000255|HAMAP-Rule:MF_00818}; OrderedLocusNames=STER_0872;
OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=322159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-491 / LMD-9;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
CC {ECO:0000255|HAMAP-Rule:MF_00818}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-
CC deazaguanine + 3 H(+) + 2 NADPH; Xref=Rhea:RHEA:13409,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:45075, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58703; EC=1.7.1.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00818};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00818}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00818}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00818}.
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DR EMBL; CP000419; ABJ66109.1; -; Genomic_DNA.
DR RefSeq; WP_002946191.1; NC_008532.1.
DR AlphaFoldDB; Q03L13; -.
DR SMR; Q03L13; -.
DR GeneID; 66898714; -.
DR KEGG; ste:STER_0872; -.
DR HOGENOM; CLU_102489_0_1_9; -.
DR OMA; LECKEFT; -.
DR UniPathway; UPA00392; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046857; F:oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1130.10; -; 1.
DR HAMAP; MF_00818; QueF_type1; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR029500; QueF.
DR InterPro; IPR016856; QueF_type1.
DR Pfam; PF14489; QueF; 1.
DR PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1.
DR TIGRFAMs; TIGR03139; QueF-II; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
FT CHAIN 1..163
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_1000062412"
FT ACT_SITE 54
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 95..96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ SEQUENCE 163 AA; 19223 MW; 20DA2F9898E7A0D6 CRC64;
MSQQEEMKNL TLLGSKETPY IFEYSPQVLE SFDNRHADND YFIKFNCPEF TSLCPITGQP
DFASIYISYI PDQLCVESKS LKLYLFSYRN HGDFHENCIN TIGKDLVELL NPRYLEVWGK
FTPRGGISID PYYNYGRPKT KYENMAEQRL FNHDLYPENI DNR
